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The effects of thermal treatments on the antigenicity and structural properties of soybean glycinin
Journal of Food Biochemistry ( IF 4 ) Pub Date : 2021-07-26 , DOI: 10.1111/jfbc.13874
Jun Xi 1 , Lili Yao 1 , Huibin Chen 1
Affiliation  

The effects of thermal treatments on the antigenicity and structural properties of soybean glycinin were investigated. An indirect enzyme-linked immunosorbent assay (iELISA) result indicated that the antigenicity of the soybean glycinin decreased to the lowest level when the heat treatment time was 50 min and the temperature was set at 110°C. The reducing sodium dodecyl sulfate-Gel electrophoresis results showed that the heat treatment had promoted the formation of small molecular weight protein subunits and concentrated protein. The free sulfhydryl (–SH) group of glycinin had increased significantly (p < .05) under the conditions of temperature between 90 and 120°C and 40 to 50 min heat treatments. The maximum fluorescence wavelength of the intrinsic fluorescence also changed significantly when compared with the control. The circular dichroism showed that the number of disordered structures had also increased significantly. These results provided evidence that the heat-induced structural modifications of glycinin will alter the antigenicity of soybean glycinin.

中文翻译:

热处理对大豆大豆球蛋白抗原性和结构特性的影响

研究了热处理对大豆大豆球蛋白的抗原性和结构特性的影响。间接酶联免疫吸附试验(iELISA)结果表明,当热处理时间为50分钟,温度设定为110℃时,大豆甘氨酸的抗原性下降到最低水平。还原性十二烷基硫酸钠-凝胶电泳结果表明,热处理促进了小分子量蛋白质亚基和浓缩蛋白质的形成。甘氨酸的游离巯基(-SH)组显着增加(p < .05) 在 90 到 120°C 之间的温度和 40 到 50 分钟的热处理条件下。与对照相比,固有荧光的最大荧光波长也发生了显着变化。圆二色性表明无序结构的数量也显着增加。这些结果提供了证据,表明热诱导的大豆球蛋白结构修饰将改变大豆大豆球蛋白的抗原性。
更新日期:2021-09-06
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